ISOLATION AND CHARACTERIZATION OF MUTATIONS IN THE HUMAN HOLOCARBOXYLASE SYNTHETASE CDNA

被引：115

作者：

SUZUKI, Y

AOKI, Y

ISHIDA, Y

CHIBA, Y

IWAMATSU, A

KISHINO, T

NIIKAWA, N

MATSUBARA, Y

NARISAWA, K

机构：

[1] KIRIN BREWERY CO LTD, KEY TECHNOL LABS, YOKOHAMA, KANAGAWA 236, JAPAN

[2] NAGASAKI UNIV, SCH MED, DEPT HUMAN GENET, NAGASAKI 852, JAPAN

来源：

NATURE GENETICS | 1994年 / 8卷 / 02期

关键词：

D O I：

10.1038/ng1094-122

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

Holocarboxylase synthetase (HCS) plays an essential role in biotin utilization in eukaryotic cells and its deficiency causes biotin-responsive multiple carboxylase deficiency in humans. We have cloned the human HCS cDNA and show that antiserum against the recombinant protein immunoprecipitates human HCS. A one base deletion resulting in a premature termination and a missense mutation (Leu to Pro) were found in cells from siblings with HCS deficiency. Human HCS shows homology to BirA, which acts as both a biotin-[acetyl-CoA-carboxylase] ligase and a biotin repressor in E. coli, suggesting a functional relationship between the two proteins. The human HCS gene maps to chromosome 21q22.1.

引用

页码：122 / 128

页数：7

共 38 条

[1] INVITRO SYNTHESIS OF PROPIONYL-COA HOLOCARBOXYLASE BY A PARTIALLY PURIFIED MITOCHONDRIAL PREPARATION FROM BIOTIN-DEFICIENT CHICKEN LIVER [J].